Fig. 1: Activation of the epidermal growth factor receptor by autophosphorylation. Adapted from Pecorino (2008)[1]Fig. 2: Regulation of Src-kinase by autophosphorylation. Adapted from Frame (2002)[2]
Autophosphorylation is a type of post-translational modification of proteins. It is generally defined as the phosphorylation of the kinase by itself. In eukaryotes, this process occurs by the addition of a phosphate group to serine, threonine or tyrosine residues within protein kinases, normally to regulate the catalytic activity.[3][4]
Autophosphorylation may occur when a kinases' own active site catalyzes the phosphorylation reaction (cis autophosphorylation), or when another kinase of the same type provides the active site that carries out the chemistry (trans autophosphorylation). The latter often occurs when kinase molecules dimerize.[3] In general, the phosphate groups introduced are gamma phosphates from nucleoside triphosphates, most commonly ATP.[3]
^Pecorino, L 2008, 'Molecular biology of cancer', Oxford University Press Inc., New York, U.S.A
^Frame MC (Jun 2002). "Src in cancer: deregulation and consequences for cell behaviour". Biochimica et Biophysica Acta (BBA) - Reviews on Cancer. 1602 (2): 114–30. doi:10.1016/s0304-419x(02)00040-9. PMID 12020799.
^ abcPetsko, GA and Ringe, D 2009, 'Protein Structure and Function', Oxford University Press Inc., New York, U.S.A
^Summers KC, Shen F, Sierra Potchanant EA, Phipps EA, Hickey RJ, Malkas LH (2011). "Phosphorylation: the molecular switch of double-strand break repair". International Journal of Proteomics. 2011: 373816. doi:10.1155/2011/373816. PMC 3200257. PMID 22084686.
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highly conservative 13-consecutive-histidine repeat. It catalyzes its autophosphorylation on serine/threonine and tyrosine residues. It may play a significant...
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bringing the two JAKs close enough to phosphorylate each other. The JAK autophosphorylation induces a conformational change within itself, enabling it to transduce...
receptor in the endoplasmic reticulum membrane. This results in the autophosphorylation of the receptor, with the phosphate then being transferred to a phosphotransfer...
intrinsic intracellular protein-tyrosine kinase activity. As a result, autophosphorylation of several tyrosine (Y) residues in the C-terminal domain of EGFR...
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phosphate to the Spo0F Sda Blocks autophosphorylation of KinA KinB Transfers phosphate to the Spo0F KipI Blocks autophosphorylation of KinA Spo0A Activates several...
bind to the receptor. The absence of receptor activation results in autophosphorylation in the histidine kinase, CheA, at a single highly conserved histidine...
Envelope Protein E2 Does Not Inhibit PKR by Simple Competition with Autophosphorylation Sites in the RNA-Binding Domain". Journal of Virology. 75 (3): 1265–1273...
the kinase activity of these receptors, which catalyses receptor autophosphorylation and tyrosine phosphorylation of RTK substrates. A kinase is a type...
intracellular anatomical structure nucleus Biological process protein autophosphorylation protein phosphorylation phosphorylation peptidyl-serine phosphorylation...
partner of the other ErbB receptors. Dimerisation results in the autophosphorylation of tyrosine residues within the cytoplasmic domain of the receptors...
transmembrane receptor to another RTK receptor, which causes the autophosphorylation and subsequent conformational change of the homodimerized receptor...
drives the homodimerization of the receptor, which in turn causes the autophosphorylation of the tyrosine kinase segment. The tropomyosin receptor kinase A...
signal transduction pathway is composed of trigger mechanisms (e.g., autophosphorylation mechanisms) that serve as signals throughout the cell. There is also...
from the luminal domain. This causes PERK to dimerize, leading to autophosphorylation and activation. The activated PERK kinase will then phosphorylate...
possesses two functional enzymatic domains, an endonuclease and a trans-autophosphorylation kinase domain. Upon activation, IRE1α oligomerizes and carries out...
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